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@ARTICLE{Barz:865626,
      author       = {Barz, Bogdan and Loschwitz, Jennifer and Strodel, Birgit},
      title        = {{L}arge-scale, dynamin-like motions of the human guanylate
                      binding protein 1 revealed by multi-resolution simulations},
      journal      = {PLoS Computational Biology},
      volume       = {15},
      number       = {10},
      issn         = {1553-7358},
      address      = {San Francisco, Calif.},
      publisher    = {Public Library of Science},
      reportid     = {FZJ-2019-04977},
      pages        = {e1007193 -},
      year         = {2019},
      abstract     = {Guanylate binding proteins (GBPs) belong to the
                      dynamin-related superfamily and exhibit various functions in
                      the fight against infections. The functions of the human
                      guanylate binding protein 1 (hGBP1) are tightly coupled to
                      GTP hydrolysis and dimerization. Despite known crystal
                      structures of the hGBP1 monomer and GTPase domain dimer,
                      little is known about the dynamics of hGBP1. To gain a
                      mechanistic understanding of hGBP1, we performed
                      sub-millisecond multi-resolution molecular dynamics
                      simulations of both the hGBP1 monomer and dimer. We found
                      that hGBP1 is a highly flexible protein that undergoes a
                      hinge motion similar to the movements observed for other
                      dynamin-like proteins. Another large-scale motion was
                      observed for the C-terminal helix α13, providing a
                      molecular view for the α13–α13 distances previously
                      reported for the hGBP1 dimer. Most of the loops of the
                      GTPase domain were found to be flexible, revealing why GTP
                      binding is needed for hGBP1 dimerization to occur.},
      cin          = {ICS-6 / JARA-HPC},
      ddc          = {610},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / $I:(DE-82)080012_20140620$},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      Structural dynamics of murine guanylate binding proteins,
                      their dimerization and interaction with lipid bilayers
                      $(jics6a_20190501)$},
      pid          = {G:(DE-HGF)POF3-551 / $G:(DE-Juel1)jics6a_20190501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31589600},
      UT           = {WOS:000500776600052},
      doi          = {10.1371/journal.pcbi.1007193},
      url          = {https://juser.fz-juelich.de/record/865626},
}